R
Richard T. Premont
Researcher at University Hospitals of Cleveland
Publications - 175
Citations - 17318
Richard T. Premont is an academic researcher from University Hospitals of Cleveland. The author has contributed to research in topics: G protein-coupled receptor kinase & Receptor. The author has an hindex of 62, co-authored 167 publications receiving 16006 citations. Previous affiliations of Richard T. Premont include Baylor College of Medicine & Icahn School of Medicine at Mount Sinai.
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Journal ArticleDOI
Seven-transmembrane receptors.
TL;DR: This paper showed that the classical models of G-protein coupling and activation of second-messenger-generating enzymes do not fully explain seven-transmembrane receptors' remarkably diverse biological actions.
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Desensitization of g protein–coupled receptors and neuronal functions
TL;DR: An important and specific role of GRKs and beta arrestins in regulating physiological responsiveness to psychostimulants and morphine suggests potential involvement of these molecules in certain brain disorders, such as addiction, Parkinson's disease, mood disorders, and schizophrenia.
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β-Arrestin-dependent, G Protein-independent ERK1/2 Activation by the β2 Adrenergic Receptor
Sudha K. Shenoy,Matthew T. Drake,Christopher D. Nelson,Daniel A. Houtz,Kunhong Xiao,Srinivasan Madabushi,Eric Reiter,Eric Reiter,Richard T. Premont,Olivier Lichtarge,Robert J. Lefkowitz +10 more
TL;DR: It is demonstrated that the β2AR can signal to ERK via a GRK5/6-β-arrestin-dependent pathway, which is independent of G protein coupling, and GRK2, membrane translocation of which requires Gβγ release upon G protein activation, was ineffective unless it was constitutively targeted to the plasma membrane by a prenylation signal.
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The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange.
Randy A. Hall,Richard T. Premont,Chung-Wai Chow,Jeremy T. Blitzer,Julie A. Pitcher,Audrey Claing,Robert H. Stoffel,Robert H. Stoffel,Larry S. Barak,Shirish Shenolikar,Edward J. Weinman,Edward J. Weinman,Edward J. Weinman,Sergio Grinstein,Robert J. Lefkowitz +14 more
TL;DR: It is reported here a direct agonist-promoted association of the β2-adrenergic receptor with the Na+/H+ exchanger regulatory factor (NHERF), a protein that regulates the activity of the Na-H- exchanger type 3 (NHE3).
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Protein kinases that phosphorylate activated G protein-coupled receptors.
TL;DR: All GRKs appear to play the same general cellular role of desensitizing activated G protein‐coupled receptors, but utilize distinctly individual means to the same end, which are just beginning to be defined.